Evidence map›Paper›PMID 19693932›Full record

ArticleProtein science : a publication of the Protein Society2009

Structure-based design of novel Chlamydomonas reinhardtii D1-D2 photosynthetic proteins for herbicide monitoring.

Giuseppina Rea, Fabio Polticelli, Amina Antonacci, Viviana Scognamiglio, Prashant Katiyar, Sudhir A Kulkarni, Udo Johanningmeier, Maria Teresa Giardi

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 62 citations in OpenAlex.

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  17. Biosensors and their applications - A review.Journal of oral biology and craniofacial research
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Giuseppina ReaInstitute of Crystallography, Monterotondo Stazione, Rome, Italy. giuseppina.rea@mlib.ic.cnr.it
Fabio Polticelli
Amina Antonacci
Viviana Scognamiglio
Prashant Katiyar
Sudhir A Kulkarni
Udo Johanningmeier
Maria Teresa Giardi
Institute of Crystallography · ITMartin Luther University Halle-Wittenberg · DERoma Tre University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The D1-D2 heterodimer in the reaction center core of phototrophs binds the redox plastoquinone cofactors, Q(A) and Q(B), the terminal acceptors of the photosynthetic electron transfer chain in the photosystem II (PSII). This complex is the target of the herbicide atrazine, an environmental pollutant competitive inhibitor of Q(B) binding, and consequently it represents an excellent biomediator to develop biosensors for pollutant monitoring in ecosystems. In this context, we have undertaken a study of the Chlamydomonas reinhardtii D1-D2 proteins aimed at designing site directed mutants with increased affinity for atrazine. The three-dimensional structure of the D1 and D2 proteins from C. reinhardtii has been homology modeled using the crystal structure of the highly homologous Thermosynechococcus elongatus proteins as templates. Mutants of D1 and D2 were then generated in silico and the atrazine binding affinity of the mutant proteins has been calculated to predict mutations able to increase PSII affinity for atrazine. The computational approach has been validated through comparison with available experimental data and production and characterization of one of the predicted mutants. The latter analyses indicated an increase of one order of magnitude of the mutant sensitivity and affinity for atrazine as compared to the control strain. Finally, D1-D2 heterodimer mutants were designed and selected which, according to our model, increase atrazine binding affinity by up to 20 kcal/mol, representing useful starting points for the development of high affinity biosensors for atrazine.

Indexed as

Biosensing TechniquesAmino Acid SequenceAtrazineChlamydomonas reinhardtiiEnvironmental MonitoringHerbicidesMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsMutationPhotosystem II Protein ComplexSequence AlignmentAtrazineHerbicidesMutant ProteinsPhotosystem II Protein Complex

Identifiers

PMID19693932
PMCPMC2786977
OpenAlexW2128904839

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.